BIOMAT Database Logo BIOMAT Database Logo

Hemoglobin S/hemoglobin Osler: a case with 3 beta globin chains. DNA sequence (AAT) proves that Hb Osler is beta 145 Tyr-->Asn. 1996

P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota 55905, USA.

A 13-year-old African-American female with erythrocytosis and three different beta globins on electrophoresis beta A, beta S, and beta Osler, raised the possibility that one chromosome 11 might contain a duplicated beta globin gene, since there are normally only 2 beta globin genes. DNA sequence analysis showed GTG at codon 6 in exon 1, corresponding to Hb S and AAT at codon 145 in exon 3, indicating a substitution of Asn for Tyr. Thus, Hb Osler undergoes spontaneous post-translational deamidation, beta 145 Asn-->beta 145 Asp. Unmodified Hb Osler (Asn) co-migrates with Hb A on electrophoresis and co-elutes with Hb A on HPLC; therefore it has not been identified previously. All previous studies have incorrectly identified the mutation as being beta 145 (HC 2) Tyr-->Asp.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D002880 Chromosomes, Human, Pair 11 A specific pair of GROUP C CHROMOSOMES of the human chromosome classification. Chromosome 11
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005091 Exons The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA. Mini-Exon,Exon,Mini Exon,Mini-Exons
D005260 Female Females
D005914 Globins A superfamily of proteins containing the globin fold which is composed of 6-8 alpha helices arranged in a characterstic HEME enclosing structure. Globin
D006451 Hemoglobin, Sickle An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia. Hemoglobin S,Deoxygenated Sickle Hemoglobin,Deoxyhemoglobin S,Hemoglobin SS,Hemoglobin, Deoxygenated Sickle,SS, Hemoglobin,Sickle Hemoglobin,Sickle Hemoglobin, Deoxygenated
D006455 Hemoglobins, Abnormal Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains. Abnormal Hemoglobins
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Hb Osler [beta 145(HC2)Tyr-->Asp] results from posttranslational modification.
March 1997, Hemoglobin,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Polycythemia produced by hemoglobin Osler (beta-145 (HC2) Tyr yields Asp).
March 1975, The Johns Hopkins medical journal,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
The structure of hemoglobin Creteil (beta 89 Ser replaced by Asn) is similar to that of abnormal human hemoglobins having sequence changes at Tyr 145 beta.
August 1981, The Journal of biological chemistry,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Assembly of human hemoglobin (Hb) beta- and gamma-globin chains expressed in a cell-free system with alpha-globin chains to form Hb A and Hb F.
April 2002, The Journal of biological chemistry,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [beta 139(H17) Asn-->Tyr].
January 1995, Hemoglobin,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Conformation in solution of hemoglobin Osler (alpha 2 A beta 2 145 Tyr replaced by Asp).
November 1979, The Journal of biological chemistry,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
DNA sequence analysis proves Hb M-Milwaukee-2 is due to beta-globin gene codon 92 (CAC-->TAC), the presumed mutation of Hb M-Hyde Park and Hb M-Akita.
January 1998, Hemoglobin,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Structural and functional study of Hb Nancy beta 145 (HC 2) Tyr replaced by Asp. A high oxygen affinity hemoglobin.
August 1975, FEBS letters,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Leech extracellular hemoglobin: two globin strains that are akin to vertebrate hemoglobin alpha and beta chains.
December 1997, Zoological science,
P J Hutt, and M H Donaldson, and J Khatri, and V F Fairbanks, and J D Hoyer, and S N Thibodeau, and M S Moxness, and L E McMorrow, and M M Green, and R T Jones
Hemoglobin Bethesda, beta 145 (HC2) Tyr replaced by His, in a Canadian family.
August 1976, American journal of clinical pathology,
Copied contents to your clipboard!